Cargando…
Probing the Activity Modification Space of the Cysteine Peptidase Cathepsin K with Novel Allosteric Modifiers
Targeting allosteric sites is gaining increasing recognition as a strategy for modulating the activity of enzymes, especially in drug design. Here we investigate the mechanisms of allosteric regulation of cathepsin K as a representative of cysteine cathepsins and a promising drug target for the trea...
Autores principales: | Novinec, Marko, Lenarčič, Brigita, Baici, Antonio |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2014
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4153677/ https://www.ncbi.nlm.nih.gov/pubmed/25184245 http://dx.doi.org/10.1371/journal.pone.0106642 |
Ejemplares similares
-
Cysteine Cathepsin Activity Regulation by Glycosaminoglycans
por: Novinec, Marko, et al.
Publicado: (2014) -
Computational investigation of conformational variability and allostery in cathepsin K and other related peptidases
por: Novinec, Marko
Publicado: (2017) -
Kinetic Characterization of Cerium and Gallium Ions as Inhibitors of Cysteine Cathepsins L, K, and S
por: Novinec, Marko, et al.
Publicado: (2022) -
The Heparin-Binding Activity of Secreted Modular Calcium-Binding Protein 1 (SMOC-1) Modulates Its Cell Adhesion Properties
por: Klemenčič, Marina, et al.
Publicado: (2013) -
Evolutionary Analysis of Dipeptidyl Peptidase I
por: Varda, Nina, et al.
Publicado: (2022)